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dc.contributor.advisorTerrones Urio, Oihanaes
dc.contributor.advisorLandeta Díaz, Olatz ORCIDes
dc.contributor.authorGoya Grocin, Andreaes
dc.contributor.otherCSIC, UPV/EHUes
dc.contributor.otherZIENTZIA ETA TEKNOLOGIA F.eu
dc.contributor.otherF. CIENCIA Y TECNOLOGIAes
dc.date.accessioned2016-04-28T18:53:36Z
dc.date.available2016-04-28T18:53:36Z
dc.date.issued2016-04-28
dc.identifier.urihttp://hdl.handle.net/10810/18102
dc.description.abstractBCL-2 family proteins are key regulators of the mitochondrial apoptotic machinery, controlling the mitochondrial outer membrane (MOM) permeabilization (MOMP). BCL-2 related Ovarian Killer (BOK) is a poorly understood pro-apoptotic member of this protein family. It has been reported that BOK localizes predominantly (although not exclusively) at membranes of the endoplasmic reticulum and of the Golgi apparatus. However, it is unclear whether BOK also operates at the MOM to promote apoptosis, as other pro-apoptotic BCL-2 family members do. Basing on the fact that the other two BAX-like pro-apoptotic members have been reported to oligomerize in order to induce MOMP, site-directed mutagenesis was used to generate two point mutations that predictably eliminated BOK’s oligomerization capacity. Then, the effect of such mutations on BOK’s membrane activity was examined using fluorescence spectroscopy.es
dc.language.isoenges
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.subjectmitochondrial apoptosises
dc.subjectBCL-2 familyes
dc.subjectBOKes
dc.subjectoligomerizationes
dc.titleStudy on the activation mechanism of BCL-2 related ovarian killer (BOK)es
dc.typeinfo:eu-repo/semantics/bachelorThesises
dc.date.updated2015-06-23T14:19:10Zes
dc.language.rfc3066eses
dc.rights.holder© 2015, la autoraes
dc.contributor.degreeBiokimikako eta Biologia Molekularreko Graduaes
dc.identifier.gaurregister60680-667627-09es
dc.identifier.gaurassign22474-667627es


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